Broadly inhibitory antibodies to severe malaria virulence proteins.

ABSTRACT: Malaria pathology is driven by the accumulation of Plasmodium falciparum-infected erythrocytes in microvessels¹. This process is mediated by the polymorphic erythrocyte membrane protein 1 (PfEMP1) adhesion proteins of the parasite. A subset of PfEMP1 variants that bind to human endothelial protein C receptor (EPCR) through their CIDRα1 domains is responsible for severe malaria pathogenesis². A longstanding question is whether individual antibodies can recognize the large repertoire of circulating PfEMP1 variants. Here we describe two broadly reactive and inhibitory human monoclonal antibodies to CIDRα1. The antibodies isolated from two different individuals exhibited similar and consistent EPCR-binding inhibition of diverse CIDRα1 domains, representing five of the six

SUBMITTER: Reyes RA 

PROVIDER: S-EPMC12338075 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature